Toxic Mastoparan B(MP-B) which is purified from the venom of the hornet Vespa basalis is a cationic amphiphilic tetradecapeptide. MP-B and its Ala-substituted analogues were synthesized by solid phase method and the toxic peptide-membrane interactions were examined by circular dichroism(CD) spectra, fluorescence spectra, and leakage abilities in phospholipid membranes. In the presence of phospholipid vesicles, synthetic MP-B and its analogues formed amphiphilic α-helical structures, but in the buffer solution, those exhibited random coil conformation as measured by CD. Fluorescence spectra of MP-13 and its analogues which indicated the binding affinity of peptide on phospholipid vesicles showed that the replacement of Lys at position 2 and 11 with Ala caused a remarkable effect in the blue shift and that at position 2, in the leakage ability of the peptide.

• 이봉헌(부산대학교 화학과) | Bong-Hun Lee (Dept. of Chemistry, Pusan Nat'l Univ.)
• 박흥재(인제대학교 환경학과) | Heung-Jai Park (Dept. of Environmental Science, Inje Univ.)